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Protein

Basic phospholipase A2 vipoxin B chain

Gene
N/A
Organism
Vipera ammodytes meridionalis (Eastern sand viper)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Heterodimer: postsynaptic neurotoxin.
Monomer: snake venom phospholipase A2 (PLA2) that shows hemolytic activity and inhibition of platelet aggregation. The hemolytic activity occurs only in presence of fatty acids (unsaturated fatty acids facilitate induce a strong hemolytic activity, whereas saturated fatty acids induce a slight activity). The inhibition of platelet aggregation is almost maximal when aggregation is induced by collagen, and arachidonic acid, whereas it is only of 30% when the aggregation is induced by ADP. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

Miscellaneous

The B chain (not complexed with the A chain) does not induce neurotoxic symptoms, hemorrhage, organ injuries and other macroscopic changes.1 Publication

Caution

The acidic chain was originally postulated to act as an inhibitor of the basic chain.Curated

Catalytic activityi

Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi27Calcium; via carbonyl oxygenBy similarity1
Metal bindingi29Calcium; via carbonyl oxygenBy similarity1
Metal bindingi31Calcium; via carbonyl oxygenBy similarity1
Active sitei471 Publication1
Metal bindingi48CalciumBy similarity1
Active sitei891 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHemostasis impairing toxin, Hydrolase, Neurotoxin, Platelet aggregation inhibiting toxin, Postsynaptic neurotoxin, Toxin
Biological processCytolysis, Hemolysis, Lipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Basic phospholipase A2 vipoxin B chain (EC:3.1.1.4)
Short name:
svPLA2
Alternative name(s):
Phosphatidylcholine 2-acylhydrolase
Vipoxin toxic component
OrganismiVipera ammodytes meridionalis (Eastern sand viper)
Taxonomic identifieri73841 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeVipera

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 of the heterodimer is 0.7-1.2 mg/kg by intraperitoneal injection into mice and 0.9-1.3 mg/kg by intravenous injection into mice.1 Publication
LD50 of the basic component is 10-13 mg/kg by intraperitoneal injection into mice, and 2.2-3.0 mg/kg by intravenous injection into mice, corresponding to 2.4-fold and more than 10-fold the LD50 of the heterodimer, respectively.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001617121 – 122Basic phospholipase A2 vipoxin B chainAdd BLAST122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26 ↔ 115Combined sources2 Publications
Disulfide bondi28 ↔ 44Combined sources2 Publications
Disulfide bondi43 ↔ 95Combined sources2 Publications
Disulfide bondi49 ↔ 122Combined sources2 Publications
Disulfide bondi50 ↔ 88Combined sources2 Publications
Disulfide bondi57 ↔ 81Combined sources2 Publications
Disulfide bondi75 ↔ 86Combined sources2 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP14420

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of A (AC P04084) and B chains; non-covalently linked. The A chain (acidic) is non-toxic, and increases the toxicity of the B chain (basic). The A chain may act as factor stabilizing the complex structure and hence retaining its toxicity by preventing non-specific binding. Upon binding to the target membranes the A chain is postulated to dissociate.3 Publications

Protein-protein interaction databases

MINTiP14420

Structurei

Secondary structure

1122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 13Combined sources12
Helixi17 – 21Combined sources5
Beta strandi22 – 24Combined sources3
Turni25 – 27Combined sources3
Beta strandi28 – 30Combined sources3
Helixi39 – 52Combined sources14
Turni59 – 61Combined sources3
Beta strandi66 – 69Combined sources4
Beta strandi72 – 75Combined sources4
Helixi81 – 98Combined sources18
Helixi100 – 102Combined sources3
Helixi105 – 107Combined sources3
Helixi112 – 115Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AOKX-ray2.00B1-122[»]
1JLTX-ray1.40B1-122[»]
1RGBX-ray3.30A/B/K/L1-122[»]
ProteinModelPortaliP14420
SMRiP14420
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14420

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG008137

Family and domain databases

CDDicd00125 PLA2c, 1 hit
Gene3Di1.20.90.10, 1 hit
InterProiView protein in InterPro
IPR001211 PLipase_A2
IPR033112 PLipase_A2_Asp_AS
IPR016090 PLipase_A2_dom
IPR036444 PLipase_A2_dom_sf
IPR033113 PLipase_A2_His_AS
PANTHERiPTHR11716 PTHR11716, 1 hit
PfamiView protein in Pfam
PF00068 Phospholip_A2_1, 1 hit
PRINTSiPR00389 PHPHLIPASEA2
SMARTiView protein in SMART
SM00085 PA2c, 1 hit
SUPFAMiSSF48619 SSF48619, 1 hit
PROSITEiView protein in PROSITE
PS00119 PA2_ASP, 1 hit
PS00118 PA2_HIS, 1 hit

Sequencei

Sequence statusi: Complete.

P14420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NLFQFAKMIN GKLGAFSVWN YISYGCYCGW GGQGTPKDAT DRCCFVHDCC
60 70 80 90 100
YGRVRGCNPK LAIYSYSFKK GNIVCGKNNG CLRDICECDR VAANCFHQNK
110 120
NTYNKNYKFL SSSRCRQTSE QC
Length:122
Mass (Da):13,828
Last modified:January 1, 1990 - v1
Checksum:i94438F9F1285FC7D
GO

Sequence databases

PIRiA29290

Similar proteinsi

Entry informationi

Entry nameiPA2B_VIPAE
AccessioniPrimary (citable) accession number: P14420
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 23, 2018
This is version 123 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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